BMF peptide

Apoptosis is related to many diseases and development. Members in the Bcl-2 family are critical regulators of apoptosis by either inhibiting or promoting cell death. Bcl-2 homology 3 (BH3) domain is a potent death domain. BH3-only proteins, including Bad, Bid, Bik, Hrk, Bim, Noxa, and PUMA, form a growing subclass of the Bcl-2 family. A novel BH3-only protein was recently identified in human and mouse and designated Bmf (for Bcl-2-modifing factor) (1). The BH3 domain in Bmf is required both for binding to Bcl-2 proteins and for triggering apoptosis. In healthy cells, Bmf associates with the dynein light chain 2 (DLC2) component of the myosin V motors and is sequestered by the cell's actin cytoskeleton. Disruption of the actin cytoskeleton, either by depolymerization of actin filaments or by detachment of cells from the extracellular matrix, triggers release and activation of Bmf, initiating the downstream apoptotic program (1,2). Bmf is constitutively expressed in many tissues (1,2).